LRC32_HUMAN
ID LRC32_HUMAN Reviewed; 662 AA.
AC Q14392; Q86V06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Transforming growth factor beta activator LRRC32 {ECO:0000305};
DE AltName: Full=Garpin {ECO:0000303|PubMed:8180135};
DE AltName: Full=Glycoprotein A repetitions predominant {ECO:0000303|PubMed:19750484, ECO:0000303|PubMed:8180135};
DE Short=GARP {ECO:0000303|PubMed:19750484, ECO:0000303|PubMed:8180135};
DE AltName: Full=Leucine-rich repeat-containing protein 32 {ECO:0000303|PubMed:19651619};
DE Flags: Precursor;
GN Name=LRRC32 {ECO:0000303|PubMed:19651619, ECO:0000312|HGNC:HGNC:4161};
GN Synonyms=D11S833E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8180135;
RA Ollendorff V., Noguchi T., Delapeyriere O., Birnbaum D.;
RT "The GARP gene encodes a new member of the family of leucine-rich repeat-
RT containing proteins.";
RL Cell Growth Differ. 5:213-219(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18628982; DOI=10.1371/journal.pone.0002705;
RA Wang R., Wan Q., Kozhaya L., Fujii H., Unutmaz D.;
RT "Identification of a regulatory T cell specific cell surface molecule that
RT mediates suppressive signals and induces Foxp3 expression.";
RL PLoS ONE 3:E2705-E2705(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19750484; DOI=10.1002/eji.200939684;
RA Stockis J., Colau D., Coulie P.G., Lucas S.;
RT "Membrane protein GARP is a receptor for latent TGF-beta on the surface of
RT activated human Treg.";
RL Eur. J. Immunol. 39:3315-3322(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TGFB1 AND TGFB2.
RX PubMed=19651619; DOI=10.1073/pnas.0901944106;
RA Tran D.Q., Andersson J., Wang R., Ramsey H., Unutmaz D., Shevach E.M.;
RT "GARP (LRRC32) is essential for the surface expression of latent TGF-beta
RT on platelets and activated FOXP3+ regulatory T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13445-13450(2009).
RN [7]
RP SIGNAL SEQUENCE CLEAVAGE SITE, AND TISSUE SPECIFICITY.
RX PubMed=21615933; DOI=10.1186/1471-2091-12-27;
RA Chan D.V., Somani A.K., Young A.B., Massari J.V., Ohtola J., Sugiyama H.,
RA Garaczi E., Babineau D., Cooper K.D., McCormick T.S.;
RT "Signal peptide cleavage is essential for surface expression of a
RT regulatory T cell surface protein, leucine rich repeat containing 32
RT (LRRC32).";
RL BMC Biochem. 12:27-27(2011).
RN [8]
RP FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-211; CYS-350 AND CYS-436.
RX PubMed=22278742; DOI=10.1091/mbc.e11-12-1018;
RA Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
RT "GARP regulates the bioavailability and activation of TGFbeta.";
RL Mol. Biol. Cell 23:1129-1139(2012).
RN [9]
RP INTERACTION WITH LAPTM4B.
RX PubMed=26126825; DOI=10.1074/jbc.m115.655340;
RA Huygens C., Lienart S., Dedobbeleer O., Stockis J., Gauthy E., Coulie P.G.,
RA Lucas S.;
RT "Lysosomal-associated Transmembrane Protein 4B (LAPTM4B) Decreases
RT Transforming Growth Factor beta1 (TGF-beta1) Production in Human Regulatory
RT T Cells.";
RL J. Biol. Chem. 290:20105-20116(2015).
RN [10]
RP INVOLVEMENT IN CPPRDD, AND VARIANT CPPRDD 544-ARG--ALA-662 DEL.
RX PubMed=30976112; DOI=10.1038/s41431-019-0380-y;
RA Harel T., Levy-Lahad E., Daana M., Mechoulam H., Horowitz-Cederboim S.,
RA Gur M., Meiner V., Elpeleg O.;
RT "Homozygous stop-gain variant in LRRC32, encoding a TGFbeta receptor,
RT associated with cleft palate, proliferative retinopathy, and developmental
RT delay.";
RL Eur. J. Hum. Genet. 27:1315-1319(2019).
CC -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1,
CC TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in
CC a latent state during storage in extracellular space (PubMed:19750484,
CC PubMed:19651619, PubMed:22278742). Associates specifically via
CC disulfide bonds with the Latency-associated peptide (LAP), which is the
CC regulatory chain of TGF-beta, and regulates integrin-dependent
CC activation of TGF-beta (PubMed:22278742). Able to outcompete LTBP1 for
CC binding to LAP regulatory chain of TGF-beta (PubMed:22278742). Controls
CC activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory
CC T-cells (Tregs) (PubMed:19750484, PubMed:19651619). Required for
CC epithelial fusion during palate development by regulating activation of
CC TGF-beta-3 (TGFB3) (By similarity). {ECO:0000250|UniProtKB:G3XA59,
CC ECO:0000269|PubMed:19651619, ECO:0000269|PubMed:19750484,
CC ECO:0000269|PubMed:22278742}.
CC -!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the
CC Latency-associated peptide chain (LAP) regulatory chain of TGFB1,
CC leading to regulate activation of TGF-beta-1 (PubMed:19651619,
CC PubMed:22278742). Interacts with TGFB2 (PubMed:19651619). Interacts
CC with TGFB3; associates via disulfide bonds with the Latency-associated
CC peptide chain (LAP) regulatory chain of TGFB3, leading to regulate
CC activation of TGF-beta-3 (By similarity). Interacts with LAPTM4B;
CC decreases TGFB1 production in regulatory T-cells (PubMed:26126825).
CC {ECO:0000250|UniProtKB:G3XA59, ECO:0000269|PubMed:19651619,
CC ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:26126825}.
CC -!- INTERACTION:
CC Q14392; P01137: TGFB1; NbExp=2; IntAct=EBI-15796956, EBI-779636;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19651619,
CC ECO:0000269|PubMed:19750484}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell surface {ECO:0000269|PubMed:19651619,
CC ECO:0000269|PubMed:19750484}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in regulatory T-cells
CC (Tregs). {ECO:0000269|PubMed:18628982, ECO:0000269|PubMed:19750484,
CC ECO:0000269|PubMed:21615933}.
CC -!- DISEASE: Cleft palate, proliferative retinopathy, and developmental
CC delay (CPPRDD) [MIM:619074]: An autosomal recessive disorder
CC characterized by mild to severe intellectual disability with delayed or
CC absent speech, hypotonia, cleft palate, proliferative retinopathy, and
CC combined sensorineural and conductive hearing loss. Brain imaging shows
CC ventriculomegaly, widened subarachnoid spaces, partial agenesis of the
CC corpus callosum, hypoplastic cerebellar vermis, and Dandy Walker
CC malformation. {ECO:0000269|PubMed:30976112}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the LRRC32/LRRC33 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52210.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z24680; CAA80847.1; -; mRNA.
DR EMBL; BC052210; AAH52210.2; ALT_INIT; mRNA.
DR EMBL; BC070079; AAH70079.1; -; mRNA.
DR CCDS; CCDS8245.1; -.
DR PIR; S42799; S42799.
DR RefSeq; NP_001122394.1; NM_001128922.1.
DR RefSeq; NP_005503.1; NM_005512.2.
DR RefSeq; XP_005273959.1; XM_005273902.3.
DR RefSeq; XP_011543237.1; XM_011544935.2.
DR RefSeq; XP_016873016.1; XM_017017527.1.
DR PDB; 6GFF; X-ray; 3.10 A; I/J=20-628.
DR PDBsum; 6GFF; -.
DR AlphaFoldDB; Q14392; -.
DR SMR; Q14392; -.
DR BioGRID; 108885; 29.
DR DIP; DIP-48932N; -.
DR IntAct; Q14392; 10.
DR STRING; 9606.ENSP00000384126; -.
DR GuidetoPHARMACOLOGY; 2913; -.
DR GlyGen; Q14392; 5 sites.
DR iPTMnet; Q14392; -.
DR PhosphoSitePlus; Q14392; -.
DR SwissPalm; Q14392; -.
DR BioMuta; LRRC32; -.
DR DMDM; 2498405; -.
DR jPOST; Q14392; -.
DR MassIVE; Q14392; -.
DR MaxQB; Q14392; -.
DR PaxDb; Q14392; -.
DR PeptideAtlas; Q14392; -.
DR PRIDE; Q14392; -.
DR ProteomicsDB; 59974; -.
DR Antibodypedia; 45130; 323 antibodies from 30 providers.
DR DNASU; 2615; -.
DR Ensembl; ENST00000260061.9; ENSP00000260061.5; ENSG00000137507.11.
DR Ensembl; ENST00000404995.5; ENSP00000385766.1; ENSG00000137507.11.
DR Ensembl; ENST00000407242.6; ENSP00000384126.2; ENSG00000137507.11.
DR GeneID; 2615; -.
DR KEGG; hsa:2615; -.
DR MANE-Select; ENST00000260061.9; ENSP00000260061.5; NM_001128922.2; NP_001122394.1.
DR UCSC; uc001oxq.5; human.
DR CTD; 2615; -.
DR DisGeNET; 2615; -.
DR GeneCards; LRRC32; -.
DR HGNC; HGNC:4161; LRRC32.
DR HPA; ENSG00000137507; Low tissue specificity.
DR MalaCards; LRRC32; -.
DR MIM; 137207; gene.
DR MIM; 619074; phenotype.
DR neXtProt; NX_Q14392; -.
DR OpenTargets; ENSG00000137507; -.
DR PharmGKB; PA28574; -.
DR VEuPathDB; HostDB:ENSG00000137507; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162288; -.
DR HOGENOM; CLU_024194_1_0_1; -.
DR InParanoid; Q14392; -.
DR OMA; PTWNKES; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q14392; -.
DR TreeFam; TF317167; -.
DR PathwayCommons; Q14392; -.
DR SignaLink; Q14392; -.
DR BioGRID-ORCS; 2615; 16 hits in 1068 CRISPR screens.
DR ChiTaRS; LRRC32; human.
DR GenomeRNAi; 2615; -.
DR Pharos; Q14392; Tbio.
DR PRO; PR:Q14392; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14392; protein.
DR Bgee; ENSG00000137507; Expressed in right coronary artery and 136 other tissues.
DR ExpressionAtlas; Q14392; baseline and differential.
DR Genevisible; Q14392; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:UniProtKB.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR GO; GO:1901398; P:regulation of transforming growth factor beta3 activation; IEA:Ensembl.
DR GO; GO:0062009; P:secondary palate development; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 20.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW Growth factor binding; Intellectual disability; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:21615933"
FT CHAIN 20..662
FT /note="Transforming growth factor beta activator LRRC32"
FT /id="PRO_0000021615"
FT TOPO_DOM 20..627
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..48
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 50..73
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 74..95
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 98..119
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 125..145
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 150..171
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 174..195
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 198..219
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 220..240
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 244..265
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 266..286
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 316..339
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 340..363
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 364..385
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 387..408
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 411..432
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 444..465
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 467..488
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 492..513
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 515..536
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 537..558
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 571..620
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000269|PubMed:22278742"
FT DISULFID 350
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000269|PubMed:22278742"
FT VARIANT 223
FT /note="L -> V (in dbSNP:rs35033061)"
FT /id="VAR_051113"
FT VARIANT 311
FT /note="G -> A (in dbSNP:rs35130967)"
FT /id="VAR_051114"
FT VARIANT 544..662
FT /note="Missing (in CPPRDD)"
FT /evidence="ECO:0000269|PubMed:30976112"
FT /id="VAR_085139"
FT MUTAGEN 211
FT /note="C->A: Abolishes interaction with Latency-associated
FT peptide (LAP) of TGFB1; when associated with A-350."
FT /evidence="ECO:0000269|PubMed:22278742"
FT MUTAGEN 350
FT /note="C->A: Abolishes interaction with Latency-associated
FT peptide (LAP) of TGFB1; when associated with A-211."
FT /evidence="ECO:0000269|PubMed:22278742"
FT MUTAGEN 436
FT /note="C->A: Abolishes Cell surface localization without
FT affecting interaction with Latency-associated peptide (LAP)
FT of TGFB1."
FT /evidence="ECO:0000269|PubMed:22278742"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 190..195
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 403..408
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 460..465
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 558..562
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:6GFF"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:6GFF"
FT HELIX 580..584
FT /evidence="ECO:0007829|PDB:6GFF"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:6GFF"
SQ SEQUENCE 662 AA; 71979 MW; 700B93ADCDF25960 CRC64;
MRPQILLLLA LLTLGLAAQH QDKVPCKMVD KKVSCQVLGL LQVPSVLPPD TETLDLSGNQ
LRSILASPLG FYTALRHLDL STNEISFLQP GAFQALTHLE HLSLAHNRLA MATALSAGGL
GPLPRVTSLD LSGNSLYSGL LERLLGEAPS LHTLSLAENS LTRLTRHTFR DMPALEQLDL
HSNVLMDIED GAFEGLPRLT HLNLSRNSLT CISDFSLQQL RVLDLSCNSI EAFQTASQPQ
AEFQLTWLDL RENKLLHFPD LAALPRLIYL NLSNNLIRLP TGPPQDSKGI HAPSEGWSAL
PLSAPSGNAS GRPLSQLLNL DLSYNEIELI PDSFLEHLTS LCFLNLSRNC LRTFEARRLG
SLPCLMLLDL SHNALETLEL GARALGSLRT LLLQGNALRD LPPYTFANLA SLQRLNLQGN
RVSPCGGPDE PGPSGCVAFS GITSLRSLSL VDNEIELLRA GAFLHTPLTE LDLSSNPGLE
VATGALGGLE ASLEVLALQG NGLMVLQVDL PCFICLKRLN LAENRLSHLP AWTQAVSLEV
LDLRNNSFSL LPGSAMGGLE TSLRRLYLQG NPLSCCGNGW LAAQLHQGRV DVDATQDLIC
RFSSQEEVSL SHVRPEDCEK GGLKNINLII ILTFILVSAI LLTTLAACCC VRRQKFNQQY
KA
